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@article{1790208, author = {Mazur, Andrii and Prudnikova, Tanyana and Grinkevich, Pavel and Mesters, Jeroen R. and Mrazova, Daria and Chaloupková, Radka and Damborský, Jiří and Kuty, Michal and Kolenko, Petr and Kuta Smatanova, Ivana}, article_location = {Chester}, article_number = {March 2021}, doi = {http://dx.doi.org/10.1107/S2059798321000486}, keywords = {DpaA; crystallization; haloalkane dehalogenases; halogenated pollutants; tetrameric structure; oligomerization}, language = {eng}, issn = {2059-7983}, journal = {Acta Crystallographica Section D: Structural Biology}, title = {The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2}, url = {https://scripts.iucr.org/cgi-bin/paper?S2059798321000486}, volume = {77}, year = {2021} }
TY - JOUR ID - 1790208 AU - Mazur, Andrii - Prudnikova, Tanyana - Grinkevich, Pavel - Mesters, Jeroen R. - Mrazova, Daria - Chaloupková, Radka - Damborský, Jiří - Kuty, Michal - Kolenko, Petr - Kuta Smatanova, Ivana PY - 2021 TI - The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2 JF - Acta Crystallographica Section D: Structural Biology VL - 77 IS - March 2021 SP - 347-356 EP - 347-356 PB - International Union of Crystallography SN - 20597983 KW - DpaA KW - crystallization KW - haloalkane dehalogenases KW - halogenated pollutants KW - tetrameric structure KW - oligomerization UR - https://scripts.iucr.org/cgi-bin/paper?S2059798321000486 N2 - Haloalkane dehalogenases (EC 3.8.1.5) are microbial enzymes that catalyse the hydrolytic conversion of halogenated compounds, resulting in a halide ion, a proton and an alcohol. These enzymes are used in industrial biocatalysis, bioremediation and biosensing of environmental pollutants or for molecular tagging in cell biology. The novel haloalkane dehalogenase DpaA described here was isolated from the psychrophilic and halophilic bacterium Paraglaciecola agarilytica NO2, which was found in marine sediment collected from the East Sea near Korea. Gel-filtration experiments and size-exclusion chromatography provided information about the dimeric composition of the enzyme in solution. The DpaA enzyme was crystallized using the sitting-drop vapour-diffusion method, yielding rod-like crystals that diffracted X-rays to 2.0 angstrom resolution. Diffraction data analysis revealed a case of merohedral twinning, and subsequent structure modelling and refinement resulted in a tetrameric model of DpaA, highlighting an uncommon multimeric nature for a protein belonging to haloalkane dehalogenase subfamily I. ER -
MAZUR, Andrii, Tanyana PRUDNIKOVA, Pavel GRINKEVICH, Jeroen R. MESTERS, Daria MRAZOVA, Radka CHALOUPKOVÁ, Jiří DAMBORSKÝ, Michal KUTY, Petr KOLENKO a Ivana KUTA SMATANOVA. The tetrameric structure of the novel haloalkane dehalogenase DpaA from Paraglaciecola agarilytica NO2. \textit{Acta Crystallographica Section D: Structural Biology}. Chester: International Union of Crystallography, 2021, roč.~77, March 2021, s.~347-356. ISSN~2059-7983. Dostupné z: https://dx.doi.org/10.1107/S2059798321000486.
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